Collaborative Research: Study of A- and B-class dye-decolorizing peroxidases (DyPs): From molecular mechanisms to applications in dye removal and lignin degradation

有了这个奖项，化学部的生命过程化学项目资助堪萨斯州立大学的李平博士和佛罗里达州立大学的宋力凯博士研究A类和B类染料脱色过氧化物酶（DyPs）的分子机制及其结构-性质-反应性-功能（SPRF）关系。本研究结果可用于废水处理和生物燃料生产的生物催化剂的开发。拟议的研究填补了关于DyPs的关键知识空白，并指导蛋白质工程，可能导致具有增强的氧化活性的酶。这种追求使研究生和博士后学员能够获得从化学到生物学的多学科领域的专业知识，从而使他们成为成功的下一代科学家。还为一个外展计划做出了贡献，该计划鼓励来自STEM职业中代表性不足的群体的学生主修科学。 本研究旨在阐明一个新的H2 O2依赖性血红素过氧化物酶家族--DyPs的分子机制和SPRF关系。这些研究集中在TcDyP从Thermomonospora curvata和ElDyP从肠杆菌lignolyticus作为代表的A-和B-类酶从这个家庭，分别。位于酶表面上的残基，负责TcDyP的底物氧化，控制一个和两个电子的还原反应，涉及ElDyP化合物I的残基（S），以及DyPs的血红素口袋周围的循环的动力学正在研究使用结构生物学，酶学，和电子顺磁共振（EPR）的调查方法。有机合成和蛋白质工程被用来定义和调节SPRF关系。这项研究的信息不仅填补了对DyPs的基本知识空白，而且为DyPs在染料去除和木质素降解方面的应用铺平了道路。该奖项反映了NSF的法定使命，并通过使用基金会的知识价值和更广泛的影响审查标准进行评估，被认为值得支持。

With this award, the Chemistry of Life Processes Program in the Chemistry Division is funding Dr. Ping Li from Kansas State University and Dr. Likai Song from Florida State University to investigate the molecular mechanism of A- and B-class dye-decolorizing peroxidases (DyPs) and their structure-property-reactivity-function (SPRF) relationship. The results of this investigation can be used in the development of biocatalysts for wastewater treatment and biofuel production. The proposed studies fill the critical knowledge gap regarding DyPs and guide protein engineering that could lead to enzymes with enhanced oxidative activity. This pursuit allows the graduate students and postdoctoral trainees to acquire expertise in multidisciplinary areas spanning from Chemistry to Biology, thus preparing them to become successful next-generation scientists. Contributions are also made to an outreach program that encourages students from groups underrepresented in STEM careers to major in science. This research project seeks to elucidate the molecular mechanism and SPRF relationship of DyPs, a new family of H2O2-dependent heme peroxidases. The studies focus on TcDyP from Thermomonospora curvata and ElDyP from Enterobacter lignolyticus as the representatives for the A- and B-class enzymes from this family, respectively. The residues situated on the enzyme surface that are responsible for substrate oxidation in TcDyP, the residue(s) that control one- and two-electron reduction reactions that involve ElDyP compound I, and the dynamics of the loop surrounding the heme pocket in DyPs are being studied using structural biology, enzymology, and electron paramagnetic resonance (EPR) investigation methods. Organic synthesis and protein engineering are being utilized to define and modulate the SPRF relationship. Information from this study not only fills the fundamental knowledge gap on DyPs but also paves the way for DyPs' applications in dye removal and lignin degradation.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.